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• W356570253 abstract "Protein stability is an important issue for the interpretation of a wide variety of biological problems but its assessment is at times difficult. The most common parameter employed to describe protein stability is the temperature of melting, at which the populations of folded and unfolded species are identical. This parameter may yield ambiguous results. It would always be preferable to measure the whole stability curve. The calculation of this curve is greatly facilitated whenever it is possible to observe cold denaturation. Using Yfh1, one of the few proteins whose cold denaturation occurs at neutral pH and low ionic strength, we could measure the variation of its full stability curve under several environmental conditions. Here we show the advantages of gauging stability as a function of external variables using stability curves." @default.
• W356570253 created "2016-06-24" @default.
• W356570253 creator A5060783973 @default.
• W356570253 creator A5067038156 @default.
• W356570253 date "2016-01-01" @default.
• W356570253 modified "2023-10-03" @default.
• W356570253 title "Cold denaturation as a tool to measure protein stability" @default.
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• W356570253 doi "https://doi.org/10.1016/j.bpc.2015.05.007" @default.
• W356570253 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4671483" @default.
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